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Pepsin is inactive at pH 6.5 and above, however pepsin is not fully denatured or irreversibly inactivated until pH 8.0. [11] [15] Therefore, pepsin in solutions of up to pH 8.0 can be reactivated upon re-acidification. The stability of pepsin at high pH has significant implications on disease attributed to laryngopharyngeal reflux. Pepsin ...
Physiologically normal intracellular pH is most commonly between 7.0 and 7.4, though there is variability between tissues (e.g., mammalian skeletal muscle tends to have a pH i of 6.8–7.1). [4] [5] There is also pH variation across different organelles, which can span from around 4.5 to 8.0. [6] [7] pH i can be measured in a number of ...
Works best at pH 8. Elastase - cuts after Ala, Gly, Ser, or Val, unless followed by Pro. Thermolysin - cuts before Ile, Met, Phe, Trp, Tyr, or Val, unless preceded by Pro. Sometimes cuts after Ala, Asp, His or Thr. Heat stable. Pepsin - cuts before Leu, Phe, Trp or Tyr, unless preceded by Pro. Also others, quite nonspecific; works best at pH 2.
Rennet extracted from older calves (grass-fed or grain-fed) contains less or no chymosin, but a high level of pepsin and can only be used for special types of milk and cheeses. As each ruminant produces a special kind of rennet to digest the milk of its own species, milk-specific rennets are available, such as kid goat rennet for goat's milk ...
This results in a deaminated protein or peptide and a free glycan. [1] [2] PNGase F has a molecular weight of 35,500 and consists of a polypeptide chain of 314 amino acids. [3] The optimal pH for enzyme activity is 8.6. However, the activity is stable for a wide variety of conditions and reagents. PNGase F maintains 60% activity from pH 6.0 to ...
Acid phosphatase (EC 3.1.3.2, systematic name phosphate-monoester phosphohydrolase (acid optimum)) is an enzyme that frees attached phosphoryl groups from other molecules during digestion. It can be further classified as a phosphomonoesterase .
Aqion is a hydrochemistry software tool. It bridges the gap between scientific software (such like PhreeqC [1]) and the calculation/handling of "simple" water-related tasks in daily routine practice.
Studies of proteins adapted to low pH have revealed a few general mechanisms by which proteins can achieve acid stability. In most acid stable proteins (such as pepsin and the soxF protein from Sulfolobus acidocaldarius), there is an overabundance of acidic residues which minimizes low pH destabilization induced by a buildup of positive charge ...